Short‐term proteomic dynamics reveal metabolic factory for active extrafloral nectar secretion by A cacia cornigera ant‐plants

• Published in: The Plant journal : for cell and molecular biology 2013-02, Vol.73 (4), p.546-554
• Main Authors: Orona‐Tamayo, Domancar, Wielsch, Natalie, Escalante‐Pérez, María, Svatos, Ales, Molina‐Torres, Jorge, Muck, Alexander, Ramirez‐Chávez, Enrique, Ádame‐Alvarez, Rosa‐María, Heil, Martin
• Format: Article
• Language: English
• ISSN: 0960-7412; 1365-313X
• DOI: 10.1111/tpj.12052

Despite the ecological and evolutionary importance of nectar, mechanisms controlling its synthesis and secretion remain largely unknown. It is widely believed that nectar is ‘secreted phloem sap’, but current research reveals a biochemical complexity that is unlikely to stem directly from the phloem. We used the short daily peak in production of extrafloral nectar by A cacia cornigera to investigate metabolic and proteomic dynamics before, during and after 2 h of diurnal secretion. Neither hexoses nor dominating nectar proteins (nectarins) were detected in the phloem before or during nectar secretion, excluding the phloem as the direct source of major nectar components. Enzymes involved in the anabolism of sugars, amino acids, proteins, and nectarins, such as invertase, β–1,3–glucanase and thaumatin‐like protein, accumulated in the nectary directly before secretion and diminished quantitatively after the daily secretion process. The corresponding genes were expressed almost exclusively in nectaries. By contrast, protein catabolic enzymes were mainly present and active after the secretion peak, and may function in termination of the secretion process. Thus the metabolic machinery for extrafloral nectar production is synthesized and active during secretion and degraded thereafter. Knowing the key enzymes involved and the spatio‐temporal patterns in their expression will allow elucidation of mechanisms by which plants control nectar quality and quantity.